ID TUT4_MOUSE Reviewed; 1644 AA.
AC B2RX14; A2A8R8; Q3UYT6; Q5DU43;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 24-JAN-2024, entry version 112.
DE RecName: Full=Terminal uridylyltransferase 4 {ECO:0000305};
DE Short=TUTase 4;
DE EC=2.7.7.52 {ECO:0000269|PubMed:19701194};
DE AltName: Full=Zinc finger CCHC domain-containing protein 11;
GN Name=Tut4 {ECO:0000312|MGI:MGI:2445126};
GN Synonyms=Kiaa0191, Zcchc11 {ECO:0000312|MGI:MGI:2445126};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-1644.
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 753-1644.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP FUNCTION IN PRE-LET-7 URIDYLATION AND MAINTENANCE OF EMBRYONIC STEM CELL
RP PLURIPOTENCY, AND SUBCELLULAR LOCATION.
RX PubMed=19703396; DOI=10.1016/j.cell.2009.08.002;
RA Heo I., Joo C., Kim Y.-K., Ha M., Yoon M.-J., Cho J., Yeom K.-H., Han J.,
RA Kim V.N.;
RT "TUT4 in concert with Lin28 suppresses MicroRNA biogenesis through pre-
RT microRNA uridylation.";
RL Cell 138:696-708(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ASP-1026 AND ASP-1028.
RX PubMed=19701194; DOI=10.1038/ncb1931;
RA Jones M.R., Quinton L.J., Blahna M.T., Neilson J.R., Fu S., Ivanov A.R.,
RA Wolf D.A., Mizgerd J.P.;
RT "Zcchc11-dependent uridylation of microRNA directs cytokine expression.";
RL Nat. Cell Biol. 11:1157-1163(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION IN PRE-LET-7 URIDYLATION, AND MUTAGENESIS OF CYS-326 AND CYS-329.
RX PubMed=22898984; DOI=10.1261/rna.034538.112;
RA Thornton J.E., Chang H.M., Piskounova E., Gregory R.I.;
RT "Lin28-mediated control of let-7 microRNA expression by alternative TUTases
RT Zcchc11 (TUT4) and Zcchc6 (TUT7).";
RL RNA 18:1875-1885(2012).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1624, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-1026 AND ASP-1028.
RX PubMed=28792939; DOI=10.1038/nature23318;
RA Morgan M., Much C., DiGiacomo M., Azzi C., Ivanova I., Vitsios D.M.,
RA Pistolic J., Collier P., Moreira P.N., Benes V., Enright A.J.,
RA O'Carroll D.;
RT "mRNA 3' uridylation and poly(A) tail length sculpt the mammalian maternal
RT transcriptome.";
RL Nature 548:347-351(2017).
RN [12]
RP FUNCTION, DOMAIN, INTERACTION WITH LIN28A, AND RNA-BINDING.
RX PubMed=28671666; DOI=10.1038/nsmb.3428;
RA Faehnle C.R., Walleshauser J., Joshua-Tor L.;
RT "Multi-domain utilization by TUT4 and TUT7 in control of let-7
RT biogenesis.";
RL Nat. Struct. Mol. Biol. 24:658-665(2017).
CC -!- FUNCTION: Uridylyltransferase that mediates the terminal uridylation of
CC mRNAs with short (less than 25 nucleotides) poly(A) tails, hence
CC facilitating global mRNA decay (PubMed:28792939). Essential for both
CC oocyte maturation and fertility. Through 3' terminal uridylation of
CC mRNA, sculpts, with TUT7, the maternal transcriptome by eliminating
CC transcripts during oocyte growth (PubMed:28792939). Involved in
CC microRNA (miRNA)-induced gene silencing through uridylation of
CC deadenylated miRNA targets. Also functions as an integral regulator of
CC microRNA biogenesiS using 3 different uridylation mechanisms (By
CC similarity). Acts as a suppressor of miRNA biogenesis by mediating the
CC terminal uridylation of some miRNA precursors, including that of let-7
CC (pre-let-7), miR107, miR-143 and miR-200c. Uridylated miRNAs are not
CC processed by Dicer and undergo degradation. Degradation of pre-let-7
CC contributes to the maintenance of embryonic stem (ES) cell pluripotency
CC (By similarity). Also catalyzes the 3' uridylation of miR-26A, a miRNA
CC that targets IL6 transcript. This abrogates the silencing of IL6
CC transcript, hence promoting cytokine expression (PubMed:19703396). In
CC the absence of LIN28A, TUT7 and TUT4 monouridylate group II pre-miRNAs,
CC which includes most of pre-let7 members, that shapes an optimal 3' end
CC overhang for efficient processing (PubMed:28671666). Add oligo-U tails
CC to truncated pre-miRNAS with a 5' overhang which may promote rapid
CC degradation of non-functional pre-miRNA species (By similarity). May
CC also suppress Toll-like receptor-induced NF-kappa-B activation via
CC binding to T2BP (By similarity). Does not play a role in replication-
CC dependent histone mRNA degradation (By similarity). Due to functional
CC redundancy between TUT4 and TUT7, the identification of the specific
CC role of each of these proteins is difficult (PubMed:28671666,
CC PubMed:28792939, PubMed:22898984). TUT4 and TUT7 restrict
CC retrotransposition of long interspersed element-1 (LINE-1) in
CC cooperation with MOV10 counteracting the RNA chaperonne activity of
CC L1RE1. TUT7 uridylates LINE-1 mRNAs in the cytoplasm which inhibits
CC initiation of reverse transcription once in the nucleus, whereas
CC uridylation by TUT4 destabilizes mRNAs in cytoplasmic ribonucleoprotein
CC granules (By similarity). {ECO:0000250|UniProtKB:Q5TAX3,
CC ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:22898984,
CC ECO:0000269|PubMed:28671666, ECO:0000269|PubMed:28792939}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide;
CC Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173116; EC=2.7.7.52;
CC Evidence={ECO:0000269|PubMed:19701194};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with LIN28A in the presence of pre-let-7 RNA
CC (PubMed:28671666). Interacts with T2BP. Interacts with MOV10; the
CC interaction is RNA-dependent. {ECO:0000250|UniProtKB:Q5TAX3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5TAX3}. Cytoplasm
CC {ECO:0000269|PubMed:19703396}. Cytoplasm, Cytoplasmic ribonucleoprotein
CC granule {ECO:0000250|UniProtKB:Q5TAX3}. Note=Mainly cytoplasmic
CC (PubMed:19703396). Translocates into the cytoplasm following treatment
CC of the cell with LPS. Co-enriched in cytoplasmic foci with MOV10.
CC {ECO:0000250|UniProtKB:Q5TAX3, ECO:0000269|PubMed:19703396}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:19701194}.
CC -!- DOMAIN: Utilizes two multidomain functional modules during the switch
CC from monouridylation to oligouridylation. The catalytic module
CC (containing the 3 CCHC-type Zinc finger domains) is essential for both
CC activities while the Lin28-interacting module (LIM) at the N-termail
CC part is indispensable for oligouridylation.
CC {ECO:0000269|PubMed:28671666}.
CC -!- DISRUPTION PHENOTYPE: Double conditional knockouts that have deleted
CC both TUT4 and TUT7 at the secondary oocyte stage are infertile. Females
CC ovulate normal numbers of oocytes with normal morphology of antral
CC follicles but with a slight decrease in the frequency of surrounded
CC nucleolus state oocytes. Mutant oocytes are unable to support early
CC embryonic development, they fail to complete meiosis I properly.
CC {ECO:0000269|PubMed:28792939}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM23506.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM25329.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL626783; CAM23506.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL627238; CAM23506.1; JOINED; Genomic_DNA.
DR EMBL; AL627238; CAM25329.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL626783; CAM25329.1; JOINED; Genomic_DNA.
DR EMBL; BC150791; AAI50792.1; -; mRNA.
DR EMBL; AK220327; BAD90397.1; -; mRNA.
DR EMBL; AK134388; BAE22125.1; -; mRNA.
DR CCDS; CCDS18451.1; -.
DR RefSeq; NP_780681.2; NM_175472.3.
DR AlphaFoldDB; B2RX14; -.
DR SMR; B2RX14; -.
DR BioGRID; 230978; 10.
DR DIP; DIP-48571N; -.
DR IntAct; B2RX14; 1.
DR STRING; 10090.ENSMUSP00000044836; -.
DR iPTMnet; B2RX14; -.
DR PhosphoSitePlus; B2RX14; -.
DR SwissPalm; B2RX14; -.
DR EPD; B2RX14; -.
DR jPOST; B2RX14; -.
DR MaxQB; B2RX14; -.
DR PaxDb; 10090-ENSMUSP00000095538; -.
DR ProteomicsDB; 298386; -.
DR Pumba; B2RX14; -.
DR Antibodypedia; 19117; 241 antibodies from 32 providers.
DR Ensembl; ENSMUST00000043368.12; ENSMUSP00000044836.6; ENSMUSG00000034610.15.
DR GeneID; 230594; -.
DR KEGG; mmu:230594; -.
DR UCSC; uc008ubd.1; mouse.
DR AGR; MGI:2445126; -.
DR CTD; 23318; -.
DR MGI; MGI:2445126; Tut4.
DR VEuPathDB; HostDB:ENSMUSG00000034610; -.
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00940000156988; -.
DR HOGENOM; CLU_003287_0_0_1; -.
DR InParanoid; B2RX14; -.
DR OMA; HCKAKKL; -.
DR BioGRID-ORCS; 230594; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Zcchc11; mouse.
DR PRO; PR:B2RX14; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; B2RX14; Protein.
DR Bgee; ENSMUSG00000034610; Expressed in manus and 233 other cell types or tissues.
DR ExpressionAtlas; B2RX14; baseline and differential.
DR Genevisible; B2RX14; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0050265; F:RNA uridylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0070569; F:uridylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0010587; P:miRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0010586; P:miRNA metabolic process; IMP:UniProtKB.
DR GO; GO:0001556; P:oocyte maturation; IMP:UniProtKB.
DR GO; GO:1990074; P:polyuridylation-dependent mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:UniProtKB.
DR GO; GO:0031054; P:pre-miRNA processing; ISS:UniProtKB.
DR GO; GO:0031664; P:regulation of lipopolysaccharide-mediated signaling pathway; IDA:MGI.
DR GO; GO:0141008; P:retrotransposon silencing by mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0071076; P:RNA 3' uridylation; IDA:UniProtKB.
DR GO; GO:0031123; P:RNA 3'-end processing; IDA:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
DR CDD; cd05402; NT_PAP_TUTase; 2.
DR Gene3D; 1.10.1410.10; -; 2.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR045100; TUTase_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR PANTHER; PTHR12271:SF49; TERMINAL URIDYLYLTRANSFERASE 4; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF03828; PAP_assoc; 2.
DR Pfam; PF19088; TUTase; 1.
DR Pfam; PF00098; zf-CCHC; 2.
DR SMART; SM00343; ZnF_C2HC; 3.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 2.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 2.
DR PROSITE; PS50158; ZF_CCHC; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Magnesium; Manganese; Metal-binding; Methylation;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-mediated gene silencing; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1644
FT /note="Terminal uridylyltransferase 4"
FT /id="PRO_0000385330"
FT DOMAIN 649..698
FT /note="PAP-associated 1"
FT DOMAIN 1201..1254
FT /note="PAP-associated 2"
FT ZN_FING 324..354
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT ZN_FING 930..947
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 1310..1327
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 1358..1375
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 30..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..353
FT /note="Required for interaction with LIN28A and pre-let-7
FT RNA"
FT /evidence="ECO:0000250|UniProtKB:Q5TAX3"
FT REGION 603..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..1634
FT /note="Sufficient for monouridylation activity"
FT /evidence="ECO:0000250|UniProtKB:Q5VYS8"
FT REGION 1329..1350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1402..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1455
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q5TAX3"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q5TAX3"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q5TAX3"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q5TAX3"
FT BINDING 1015..1018
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q5VYS8"
FT BINDING 1025..1028
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q5VYS8"
FT BINDING 1026
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 1028
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 1098
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q5VYS8"
FT BINDING 1120
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q5VYS8"
FT BINDING 1138..1142
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q5VYS8"
FT BINDING 1254
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q5VYS8"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5TAX3"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1624
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MUTAGEN 326
FT /note="C->A: No effect on basal uridylation activity, but
FT loss of LIN28A-enhanced uridylation; when associated with
FT A-329."
FT /evidence="ECO:0000269|PubMed:22898984"
FT MUTAGEN 329
FT /note="C->A: No effect on basal uridylation activity, but
FT loss of LIN28A-enhanced uridylation; when associated with
FT A-326."
FT /evidence="ECO:0000269|PubMed:22898984"
FT MUTAGEN 1026
FT /note="D->A: Loss of nucleotidyltransferase activity and
FT oocytes are unable to support early embryonic development;
FT when associated with A-1028."
FT /evidence="ECO:0000269|PubMed:19701194,
FT ECO:0000269|PubMed:28792939"
FT MUTAGEN 1028
FT /note="D->A: Loss of nucleotidyltransferase activity and
FT oocytes are unable to support early embryonic development;
FT when associated with A-1026."
FT /evidence="ECO:0000269|PubMed:19701194,
FT ECO:0000269|PubMed:28792939"
FT CONFLICT 815
FT /note="D -> A (in Ref. 2; AAI50792 and 3; BAD90397)"
FT /evidence="ECO:0000305"
FT CONFLICT 1336
FT /note="S -> R (in Ref. 4; BAE22125)"
FT /evidence="ECO:0000305"
FT CONFLICT 1422
FT /note="S -> C (in Ref. 4; BAE22125)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1644 AA; 184650 MW; 5EE701412E6157A0 CRC64;
MEEPKTSKNE NHEPKKNIIC EESKAVKIIS NQTLKPRNDK SEIGTSSLNR NSSKKTKQND
ICIEKTEAKS CKVNAASVPG PKDLGLVHRD QSHCKMKKLP NSPMKAQKGS SQTKLEKTPS
LQTKAEKVPK SPNLPVKAEK APCTTAEATT EKALNSQRKE ENTPTSQMKL QKTPRSPLEP
ENVPSLLLKE NVKQTESQQT GKKLTSSFVS MDKRKSEALQ GEKSALENSS LSQKQQTQTD
NIADSDDSAS GIEDTADDLS KMKSEESNKE NSSEMDYLEN ATVIDESALT PEQRLGLKQA
EERLERDHIF RLEKRSPEYT NCRYLCKLCL IHIENIQGAH KHIKEKRHKK NILEKQEESE
LRSLPSPSSA HLAALSVAVV ELAKEQGITD DDLRIRQDIV EEMSKVIMTF LPECSLRLYG
SSLTKFALKS SDVNIDIKFP PKMNHPDLLI QVLGILKKSA LYIDVESDFH AKVPVVVCKD
RKSALLCRVS AGNDMACLTT DLLAALGKVE PVFTPLVLAF RYWAKLCYID SQTDGGIPSY
CFALMVMFFL QQRKPPLLPC LLGSWIEGFD PKRMDDFQLK GIVEEKFVKW EYNSSSATEK
NLIADENKAK ADEPKDDTKK TETDNQSNAA KAKHGKSPLT LEAPNQVPLG QLWLELLKFY
TLDFALEEYV ICVRIQDILT RENKNWPKRR IAIEDPFSVK RNVARSLNSQ LVYEYVVERF
RAAYRYFACP QKKGGNKSTM DPKKKEKGKL SSKKPVKSDC SATNCCILGE SAEKIHMERG
QPAKHDETEF TSQRCIVDND SLLVNELGLA NHGQDSSSLS TASGGSDLKQ KSAEKQGDLT
PSETSLKKEL SQCICIGTPD GAESAGTDCR SNLEMDSSHQ IVCNNVSATS CNCKATEVTS
DLVDEDNLPS QELYYVFDKF ILTSGKPPTI VCSICKKDGH SKNDCPEDFR KIDLKPLPPM
TNRFREILDL VCKRCFDELS PPCSEQHNRE QILIGLEKFI QKEYDEKARL CLFGSSKNGF
GFRDSDLDIC MTLEGHENAE KLNCKEIIEN LAKILKRHPG LRNILPITTA KVPIVKFEHR
RSGLEGDISL YNTLAQHNTR MLATYAAIDP RVQYLGYTMK VFAKRCDIGD ASRGSLSSYA
YILMVLYFLQ QRKPPVIPVL QEIFDGKQIP QRMVDGWNAF FFDKTEELKK RLPSLGKNTE
SLGELWLGLL RFYTEEFDFK EYVISIRQKK LLTTFEKQWT SKCIAIEDPF DLNHNLGAGV
SRKMTNFIMK AFINGRKLFG TPFYPLIGRE AEYFFDSRVL TDGELAPNDR CCRVCGKIGH
YMKDCPKRKR LKKKDSEEEK EGNEEEKDSR DLLDSRDLRC FICGDAGHVR RECPEVKMAR
QRNSSVAAAQ LVRNLVNAQQ VAGSAQQQSD QSIRTRQSSE CSDSPSYSPQ PQPFPQNSPQ
PSALPPPPSQ PGSQPKLGPP QQGGQPPHQV QMPLYNFPQS PPAHYSPMHS MGLLPMHPLQ
IPAPSWPIHG PMLHSAPGST PSNIGLNDPS IIFAQPAARP MAIPSPSHDG HWPRTVAPNS
LVNNGAVGNS EPRFRGLNPP IPWEHAPRHF PLVPASWPYG LHQNFMHQGN PRFQPKPFYA
QADRCATRRC RERCPHPPRG NVSE
//
